Figure_6.tif (2.49 MB)
Download file

Overall structural comparison of DmcN-IIIB bound to m7G with MmcN-IIIA bound to UMP.

Download (0 kB)
figure
posted on 06.03.2014, 04:27 by Thomas Monecke, Juliane Buschmann, Piotr Neumann, Elmar Wahle, Ralf Ficner

Superposition of DmcN-IIIB (HAD core in white; cap domain in red) and cN-IIIA (HAD core in grey; cap domain in blue) showing the overall structural similarity of both enzymes. Note that the cap domain of cN-IIIB is shifted by 4 Å when the structures are superposed via their the HAD core. Thus, the substrate-bound cN-IIIA adopts a closed conformation while the product-bound cN-IIIB represents an open conformation. A movie of the trajectory from the open-to-closed state is shown in Movie S1.

History